| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EPHX2 | NADSYN1 | ENSP00000430269 | ENSP00000326424 | Bifunctional epoxide hydrolase 2; Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady- state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10- phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10- phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z- enoic acid and 12-phospho [...] | Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.491 |
| EPHX2 | NT5E | ENSP00000430269 | ENSP00000257770 | Bifunctional epoxide hydrolase 2; Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady- state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10- phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10- phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z- enoic acid and 12-phospho [...] | 5'-nucleotidase; Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities. | 0.795 |
| EPHX2 | NUDT13 | ENSP00000430269 | ENSP00000349874 | Bifunctional epoxide hydrolase 2; Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady- state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10- phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10- phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z- enoic acid and 12-phospho [...] | Nucleoside diphosphate-linked moiety X motif 13; Nudix hydrolase 13. | 0.842 |
| EPHX2 | NUDT15 | ENSP00000430269 | ENSP00000258662 | Bifunctional epoxide hydrolase 2; Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady- state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10- phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10- phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z- enoic acid and 12-phospho [...] | Nucleotide triphosphate diphosphatase NUDT15; May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives. Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides t [...] | 0.484 |
| EPHX2 | PSPH | ENSP00000430269 | ENSP00000378854 | Bifunctional epoxide hydrolase 2; Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady- state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10- phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10- phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z- enoic acid and 12-phospho [...] | Phosphoserine phosphatase; Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates; Belongs to the HAD-like hydrolase superfamily. SerB family. | 0.432 |
| HDDC2 | NUDT13 | ENSP00000381220 | ENSP00000349874 | HD domain containing 2. | Nucleoside diphosphate-linked moiety X motif 13; Nudix hydrolase 13. | 0.792 |
| NADSYN1 | EPHX2 | ENSP00000326424 | ENSP00000430269 | Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | Bifunctional epoxide hydrolase 2; Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady- state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10- phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10- phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z- enoic acid and 12-phospho [...] | 0.491 |
| NADSYN1 | NT5E | ENSP00000326424 | ENSP00000257770 | Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 5'-nucleotidase; Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities. | 0.826 |
| NADSYN1 | NUDT13 | ENSP00000326424 | ENSP00000349874 | Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | Nucleoside diphosphate-linked moiety X motif 13; Nudix hydrolase 13. | 0.822 |
| NADSYN1 | NUDT15 | ENSP00000326424 | ENSP00000258662 | Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | Nucleotide triphosphate diphosphatase NUDT15; May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives. Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides t [...] | 0.899 |
| NT5C | NT5E | ENSP00000245552 | ENSP00000257770 | 5'(3')-deoxyribonucleotidase, cytosolic type; Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP. | 5'-nucleotidase; Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities. | 0.936 |
| NT5C | NUDT13 | ENSP00000245552 | ENSP00000349874 | 5'(3')-deoxyribonucleotidase, cytosolic type; Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP. | Nucleoside diphosphate-linked moiety X motif 13; Nudix hydrolase 13. | 0.587 |
| NT5E | EPHX2 | ENSP00000257770 | ENSP00000430269 | 5'-nucleotidase; Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities. | Bifunctional epoxide hydrolase 2; Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady- state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10- phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10- phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z- enoic acid and 12-phospho [...] | 0.795 |
| NT5E | NADSYN1 | ENSP00000257770 | ENSP00000326424 | 5'-nucleotidase; Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities. | Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. | 0.826 |
| NT5E | NT5C | ENSP00000257770 | ENSP00000245552 | 5'-nucleotidase; Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities. | 5'(3')-deoxyribonucleotidase, cytosolic type; Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP. | 0.936 |
| NT5E | NUDT13 | ENSP00000257770 | ENSP00000349874 | 5'-nucleotidase; Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities. | Nucleoside diphosphate-linked moiety X motif 13; Nudix hydrolase 13. | 0.808 |
| NT5E | NUDT15 | ENSP00000257770 | ENSP00000258662 | 5'-nucleotidase; Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities. | Nucleotide triphosphate diphosphatase NUDT15; May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives. Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides t [...] | 0.813 |
| NUDT1 | NUDT13 | ENSP00000380241 | ENSP00000349874 | 7,8-dihydro-8-oxoguanine triphosphatase; Antimutagenic. Plays a redundant role in sanitizing oxidized nucleotide pools, such as 8-oxo-dGTP pools. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8- oxo-GTP and 8-oxo-ATP. Does not play a [...] | Nucleoside diphosphate-linked moiety X motif 13; Nudix hydrolase 13. | 0.587 |
| NUDT1 | NUDT15 | ENSP00000380241 | ENSP00000258662 | 7,8-dihydro-8-oxoguanine triphosphatase; Antimutagenic. Plays a redundant role in sanitizing oxidized nucleotide pools, such as 8-oxo-dGTP pools. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8- oxo-GTP and 8-oxo-ATP. Does not play a [...] | Nucleotide triphosphate diphosphatase NUDT15; May catalyze the hydrolysis of nucleoside triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP and the prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. Could also catalyze the hydrolysis of some nucleoside diphosphate derivatives. Hydrolyzes oxidized nucleosides triphosphates like 8-oxo-dGTP in vitro, but the specificity and efficiency towards these substrates are low. Therefore, the potential in vivo sanitizing role of this enzyme, that would consist in removing oxidatively damaged forms of nucleosides t [...] | 0.763 |
| NUDT13 | EPHX2 | ENSP00000349874 | ENSP00000430269 | Nucleoside diphosphate-linked moiety X motif 13; Nudix hydrolase 13. | Bifunctional epoxide hydrolase 2; Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady- state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10- phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10- phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z- enoic acid and 12-phospho [...] | 0.842 |